HMGN5_RAT
ID HMGN5_RAT Reviewed; 429 AA.
AC B4F777;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=High mobility group nucleosome-binding domain-containing protein 5;
DE AltName: Full=Nucleosome-binding protein 1 {ECO:0000303|PubMed:19160411};
GN Name=Hmgn5 {ECO:0000250|UniProtKB:P82970};
GN Synonyms=Nsbp1 {ECO:0000312|RGD:1597988};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAI68165.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway/NHsdMcwi {ECO:0000269|PubMed:15489334};
RC TISSUE=Embryonic brain {ECO:0000312|EMBL:AAI68165.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19160411; DOI=10.1002/jcb.22046;
RA Shirakawa H., Rochman M., Furusawa T., Kuehn M.R., Horigome S., Haketa K.,
RA Sugita Y., Inada T., Komai M., Bustin M.;
RT "The nucleosomal binding protein NSBP1 is highly expressed in the placenta
RT and modulates the expression of differentiation markers in placental Rcho-1
RT cells.";
RL J. Cell. Biochem. 106:651-658(2009).
CC -!- FUNCTION: Preferentially binds to euchromatin and modulates cellular
CC transcription by counteracting linker histone-mediated chromatin
CC compaction. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9JL35}.
CC Note=Associates with nucleosomes in euchromatin and is largely excluded
CC from constitutive heterochromatin. {ECO:0000250|UniProtKB:Q9JL35}.
CC -!- TISSUE SPECIFICITY: Expressed in trophoblast giant cells.
CC {ECO:0000269|PubMed:19160411}.
CC -!- INDUCTION: Up-regulated in differentiated trophoblast giant cells.
CC {ECO:0000269|PubMed:19160411}.
CC -!- DOMAIN: Specifically targeted by its C-terminus to nucleosomes in
CC euchromatin. {ECO:0000250|UniProtKB:Q9JL35}.
CC -!- SIMILARITY: Belongs to the HMGN family. {ECO:0000255}.
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DR EMBL; BC168165; AAI68165.1; -; mRNA.
DR RefSeq; NP_001128178.1; NM_001134706.1.
DR AlphaFoldDB; B4F777; -.
DR BioGRID; 596215; 1.
DR STRING; 10116.ENSRNOP00000047671; -.
DR iPTMnet; B4F777; -.
DR PhosphoSitePlus; B4F777; -.
DR jPOST; B4F777; -.
DR PaxDb; B4F777; -.
DR PeptideAtlas; B4F777; -.
DR PRIDE; B4F777; -.
DR GeneID; 681284; -.
DR UCSC; RGD:1597988; rat.
DR CTD; 681284; -.
DR RGD; 1597988; Hmgn5.
DR VEuPathDB; HostDB:ENSRNOG00000029078; -.
DR eggNOG; ENOG502SUX9; Eukaryota.
DR HOGENOM; CLU_685059_0_0_1; -.
DR InParanoid; B4F777; -.
DR OMA; IFTQGQF; -.
DR OrthoDB; 728724at2759; -.
DR TreeFam; TF105374; -.
DR PRO; PR:B4F777; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000029078; Expressed in ovary and 19 other tissues.
DR Genevisible; B4F777; RN.
DR GO; GO:0000785; C:chromatin; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR InterPro; IPR040164; HMGN5.
DR InterPro; IPR000079; HMGN_fam.
DR PANTHER; PTHR23145; PTHR23145; 1.
DR Pfam; PF01101; HMG14_17; 1.
DR PRINTS; PR00925; NONHISHMG17.
DR SMART; SM00527; HMG17; 1.
DR PROSITE; PS00355; HMG14_17; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..429
FT /note="High mobility group nucleosome-binding domain-
FT containing protein 5"
FT /id="PRO_0000390932"
FT REGION 1..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P82970"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82970"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P82970"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P82970"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P82970"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P82970"
SQ SEQUENCE 429 AA; 48605 MW; EDDEC01ECC676BF1 CRC64;
MPKRKAAGDA SQEPKRRSAR LSAMPVPFTP ELKPKRASTS RKTKTTNVVE ESKDAGATTI
PETKPEVVKG ECNMENAENG EAKIIEAPIS KMETEEVKEQ INEDTEGDGG EKKEAVVTKG
KNDELEANIQ DVEKDEDEKE HEDTGEEGED GEREGGLKEK PDVAEIEDAK EAKDDEEKED
KEKEDDKGGD GKKEEEKDDE GEAETEEEVK EQQKEETEGD DGKCKVEENK EGRKESQHEE
EGKEELHEED GKEDLHEEDG KEDLHEEDGK EDLHEEEGKE DLHEEEGKED LHEEEGKEDL
HEEEGKEDLH EEEGKEDLHE EEGKEDLHEE EGKEDLHEED GKEGQHEEEG KEDLHEEEGK
EDLHEEDGKE GQHEEDGKKK ADGNEDRKEE EEQEAATEGN DENKVEVEEE ADNKDFKEDG
EKGEPVSTV
